This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. Allostery describes altered protein function at one site due to a perturbation at another site. One mechanism of allostery involves correlated motions, which can occur even in the absence of substantial conformational change. We present a novel method, "MutInf", to identify statistically significant correlated motions from equilibrium molecular dynamics simulations. We then applied this method to a number of proteins to provide insights into allosteric mechanisms and identify novel allosteric pathways, proteins such as interleukin-2, ubiquitin conjugating enzyme (E2) UBCH5B, the Pin-1 WW domain, and caspase-1. We also have developed a novel method of comparing conformational ensembles from molecular dynamics simulations using an information-theoretic metric, and have applied this to examine post-translational modifications and allostery.